5HFK
CRYSTAL STRUCTURE OF A GLUTATHIONE S-TRANSFERASE PROTEIN FROM ESCHERICHIA COLI OCh 157:H7 STR. SAKAI (ECs3186, TARGET EFI-507414) WITH BOUND GLUTATHIONE
Functional Information from GO Data
| Chain | GOid | namespace | contents |
| A | 0004601 | molecular_function | peroxidase activity |
| A | 0006979 | biological_process | response to oxidative stress |
| A | 0015036 | molecular_function | disulfide oxidoreductase activity |
| A | 0042803 | molecular_function | protein homodimerization activity |
| A | 0098869 | biological_process | cellular oxidant detoxification |
| B | 0004601 | molecular_function | peroxidase activity |
| B | 0006979 | biological_process | response to oxidative stress |
| B | 0015036 | molecular_function | disulfide oxidoreductase activity |
| B | 0042803 | molecular_function | protein homodimerization activity |
| B | 0098869 | biological_process | cellular oxidant detoxification |
Functional Information from PDB Data
| site_id | AC1 |
| Number of Residues | 13 |
| Details | binding site for residue GSH A 301 |
| Chain | Residue |
| A | ASN11 |
| A | HOH477 |
| A | HOH501 |
| B | ARG132 |
| B | HOH430 |
| A | GLY109 |
| A | PRO110 |
| A | GLY113 |
| A | TRP169 |
| A | GSH302 |
| A | HOH416 |
| A | HOH428 |
| A | HOH474 |
| site_id | AC2 |
| Number of Residues | 16 |
| Details | binding site for residue GSH A 302 |
| Chain | Residue |
| A | THR9 |
| A | ASN11 |
| A | GLN38 |
| A | ASN50 |
| A | LYS51 |
| A | ILE52 |
| A | PRO53 |
| A | GLU71 |
| A | SER72 |
| A | GSH301 |
| A | HOH423 |
| A | HOH428 |
| A | HOH467 |
| A | HOH476 |
| A | HOH482 |
| A | HOH535 |
| site_id | AC3 |
| Number of Residues | 13 |
| Details | binding site for residue GSH B 301 |
| Chain | Residue |
| A | ARG132 |
| A | HOH459 |
| B | ASN11 |
| B | GLY109 |
| B | PRO110 |
| B | GLY113 |
| B | TRP169 |
| B | GSH302 |
| B | HOH418 |
| B | HOH427 |
| B | HOH463 |
| B | HOH465 |
| B | HOH492 |
| site_id | AC4 |
| Number of Residues | 16 |
| Details | binding site for residue GSH B 302 |
| Chain | Residue |
| B | THR9 |
| B | ASN11 |
| B | GLN38 |
| B | ASN50 |
| B | LYS51 |
| B | ILE52 |
| B | PRO53 |
| B | GLU71 |
| B | SER72 |
| B | GSH301 |
| B | HOH418 |
| B | HOH431 |
| B | HOH443 |
| B | HOH474 |
| B | HOH486 |
| B | HOH516 |
Functional Information from SwissProt/UniProt
| site_id | SWS_FT_FI1 |
| Number of Residues | 10 |
| Details | BINDING: BINDING => ECO:0000269|PubMed:19537707 |
| Chain | Residue | Details |
| A | ASN11 | |
| B | ARG132 | |
| A | GLN38 | |
| A | ILE52 | |
| A | GLU71 | |
| A | ARG132 | |
| B | ASN11 | |
| B | GLN38 | |
| B | ILE52 | |
| B | GLU71 |
| site_id | SWS_FT_FI2 |
| Number of Residues | 2 |
| Details | BINDING: BINDING => ECO:0000250|UniProtKB:P08263 |
| Chain | Residue | Details |
| A | ARG40 | |
| B | ARG40 |
